CN116082499B - 一种抗登革ns1蛋白的抗体及其应用 - Google Patents
一种抗登革ns1蛋白的抗体及其应用 Download PDFInfo
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Abstract
本发明涉及一种抗登革NS1蛋白的抗体及其制备方法和用途。本发明制备的抗登革NS1蛋白的单克隆抗体对抗登革NS1蛋白具有高亲和性、高反应活性、高灵敏度和特异性,为登革热疾病的诊断提供了重要的原料来源。
Description
技术领域
本发明属于抗体技术领域。更具体地,涉及一种抗登革NS1蛋白的抗体及其应用。
背景技术
登革热(dengue fever,DF)是由4个血清型病毒(DENV-1、DENV-2、DENV-3、DENV-4)引起的急性蚊媒传染病,主要通过埃及伊蚊和白纹伊蚊传播DF是分布最广,发病最多,危害较大的一种虫媒病毒性疾病,广泛流行于全球热带和亚热带的非洲、美洲、东南亚和西太平洋地区的100多个国家和地区。
登革热没有特效的治疗方法。如果没有适应的治疗,登革出血热的病死率可超过20%,经过有效的支持疗法,病死率可低于1%。登革热诊断要点:1)流行病学资料,发病关15天的活动情况,有否去过流行区,蚊虫叮咬历;2)临床特征,突然起病,发热,“三痛三红”,皮诊;3)实验室检查,白细胞、血小板下降;检测血清特性IgM阳性;恢复期IgG比急性期有4倍增长;分离到病毒或特异性抗原。临床上用于登革病毒的检测方法有病毒培养、血清学检测、病毒核酸检测等。病毒分离所需时间较长,达不到快速诊断的目的,而常规的血清学诊断又因存在广泛的交叉反应而受到干扰。胶体金标记的免疫层析方法具有快速、简便、不需要依赖重要装备、能够实现现场检测等特点,成为目前传染病快速诊断中研究的热点。
NS1蛋白是登革病毒非结构蛋白中唯一的糖蛋白,抗原性极强且不引发抗体信赖性感染增强现象(Antibody-dependent enhancement,ADE),所以作为胶体金检测的靶标。而胶体金检测需要针对NS1蛋白的特异性单克隆抗体,传统临床用的都是鼠源性的单克隆抗体。现在市场主流抗登革NS1的单克隆抗体原料来源于进口,价格高,特异性、灵敏度都有待提升。
鉴于此,特提出本发明。
发明内容
本发明要解决的技术问题是克服现有抗登革NS1的单克隆抗体原料特异性及灵敏度的缺陷问题,本发明制备的抗登革NS1蛋白的抗体亲和力、反应活性、特异性及灵敏度方面明显优于市场主流抗体。
本发明的目的是提供一种抗体或抗原结合片段,所述抗体或抗原结合片段含有以下CDRs:
HCDR1,其包含SEQ ID NO.1所示的氨基酸序列,或由其组成;
HCDR2,其包含SEQ ID NO.2所示的氨基酸序列,或由其组成;
HCDR3,其包含SEQ ID NO.3或SEQ ID NO.19所示的氨基酸序列,或由SEQ ID NO.3或SEQ ID NO.19所示的氨基酸序列组成;
LCDR1,其包含SEQ ID NO.4所示的氨基酸序列,或由其组成;
LCDR2,其包含SEQ ID NO.5所示的氨基酸序列,或由其组成;
LCDR3,其包含SEQ ID NO.6所示的氨基酸序列,或由其组成。
本发明的另一目的是提供一种抗体或抗原结合片段,所述抗体或抗原结合片段包含重链可变区和轻链可变区,所述重链可变区包含上述的HCDR1-3,所述轻链可变区包含上述的LCDR1-3。
本发明的另一目的是提供所述抗体或抗原结合片段相关的核酸、载体或细胞。
本发明还提供了制备所述抗体或抗原结合片段的方法。
本发明还提供了一种抗体偶联物,以及包含上述抗体或抗原结合片段或所述抗体偶联物的试剂盒/诊断试剂。
本发明还提供了所述抗体或抗原结合片段或所述抗体偶联物在制备试剂盒或诊断试剂中的用途。
附图说明
图1是DF-5M32RMb1抗体的还原性SDS-PAGE结果。
具体实施方式
以下结合具体实施例来进一步说明本发明,但实施例并不对本发明做任何形式的限定。除非特别说明,本发明采用的试剂、方法和设备为本技术领域常规试剂、方法和设备。
除非特别说明,以下实施例所用试剂和材料均为市购。
本发明涉及一种抗体或抗原结合片段,所述抗体或抗原结合片段包含以下CDRs:
HCDR1,其包含SEQ ID NO.1所示的氨基酸序列,或由其组成;
HCDR2,其包含SEQ ID NO.2所示的氨基酸序列,或由其组成;
HCDR3,其包含SEQ ID NO.3或SEQ ID NO.19所示的氨基酸序列,或由SEQ ID NO.3或SEQ ID NO.19所示的氨基酸序列组成;
LCDR1,其包含SEQ ID NO.4所示的氨基酸序列,或由其组成;
LCDR2,其包含SEQ ID NO.5所示的氨基酸序列,或由其组成;
LCDR3,其包含SEQ ID NO.6所示的氨基酸序列,或由其组成。
在本发明中,术语“抗体”在最广义上使用,其可以包括全长单克隆抗体,双特异性或多特异性抗体,以及嵌合抗体,只要它们展示所需的生物学活性。术语“抗原结合片段”是包含抗体CDR的一部分或全部的物质,其缺乏至少一些存在于全长链中的氨基酸但仍能够特异性结合至抗原。此类片段具生物活性,因为其结合至抗原,且可与其他抗原结合分子(包括完整抗体)竞争结合至给定表位。此类片段选自Fab(由完整的轻链和Fd构成),Fv(由VH和VL构成),scFv(单链抗体,VH和VL之间由一连接肽连接而成)或单域抗体(仅由VH组成)。此类片段可通过重组核酸技术产生,或可通过抗原结合分子(包括完整抗体)的酶裂解或化学裂解产生。
在本发明中,术语“互补性决定区”、“CDR”或“CDRs”是指免疫球蛋白的重链和轻链的高度可变区,指包含一种或多种或者甚至全部的对抗体或抗原结合片段与其识别的抗原或表位的结合亲和力起作用的主要氨基酸残基的区域。在本发明具体实施方式中,CDRs是指所述抗体的重链和轻链的高度可变区。
在本发明中,重链互补决定区用HCDR表示,其包括HCDR1、HCDR2和HCDR3;轻链互补决定区用LCDR表示,其包括LCDR1、LCDR2和LCDR3。本领域常用的CDR标示方法包括:Kabat编号方案、IMGT编号方案、Chothia和Lesk编号方案以及1997年Lefranc等人为免疫球蛋白超家族的所有蛋白质序列引入的新的标准化编号***。Kabat等人是第一个为免疫球蛋白可变区提出标准化编号方案的人。在过去的几十年中,序列的积累导致了KABATMAN数据库的创建,Kabat编号方案通常被认为是编号抗体残基广泛采用的标准。本发明采用Kabat注释标准标示CDR区,但其他方法标示的CDR区也属于本发明的保护范围。
在本发明中,“框架区”或“FR”区包括重链框架区和轻链框架区,是指抗体重链可变区和轻链可变区中除CDR之外的区域;其中,重链框架区可以被进一步细分成被CDR分隔开的毗邻区域,包含HFR1、HFR2、HFR3和HFR4框架区;轻链框架区可以被进一步细分成被CDR分隔开的毗邻区域,包含HFR1、HFR2、HFR3和HFR4框架区。
在本发明中,重链可变区由以下编号的CDR与FR按如下组合排列连接获得:HFR1-HCDR1-HFR2-HCDR2-HFR3-HCDR3-HFR4;轻链可变区由以下编号的CDR与FR按如下组合排列连接获得:LFR1-LCDR1-LFR2-LCDR2-LFR3-LCDR3-LFR4。
在一些实施方式中,所述抗体还包含重链可变区的框架区HFR1、HFR2、HFR3和HFR4,和轻链可变区的框架区LFR1、LFR2、LFR3和LFR4,其中:
HFR1包含SEQ ID NO:7或SEQ ID NO:20任一氨基酸序列,或由其组成;
HFR2-4依次包含SEQ ID NO:8-10的氨基酸序列,或依次由SEQ ID NO:8-10的氨基酸序列组成;
LFR1-4依次包含SEQ ID NO:11-14的氨基酸序列,或依次由SEQ ID NO:11-14的氨基酸序列组成。
需要说明的是,在其他的实施例中,本发明提供的抗体或抗原结合片段的各框架区氨基酸序列可以与上述对应框架区(SEQ ID NO:7、8、9、10、11、12、13或14)具有至少80%、81%、82%、83%、84%、85%、86%、87%、88%、89%、90%、91%、92%、93%、94%、95%、96%、97%、98%或99%的同源性。
在一些实施方式中,所述的抗体或抗原结合片段的结合亲和力KD≤6.36*10-8M。
第二方面,本发明涉及一种抗体或抗原结合片段,所述抗体或抗原结合片段包含重链可变区和/或轻链可变区,所述重链可变区包含上述的HCDR1-3和上述的HFR1-4,所述轻链可变区包含上述的LCDR1-3和上述的LFR1-4。
在一些实施方式中,所述重链可变区包含选自SEQ ID NO:15、SEQ ID NO:21-23任一所示的氨基酸序列;所述轻链可变区包含SEQ ID NO:16所示的氨基酸序列。
在一些实施方式中,所述重链可变区的氨基酸序列由SEQ ID NO:15、SEQ ID NO:21-23任一所示的氨基酸序列组成;所述轻链可变区由SEQ ID NO:16所示的氨基酸序列组成。
在一些实施方式中,所述抗体还包含恒定区;
在一些实施方式中,所述恒定区包括重链恒定区和/或轻链恒定区;
在一些实施方式中,所述重链恒定区选自IgG1、IgG2、IgG3、IgG4、IgA、IgM、IgE或IgD的重链恒定区;所述轻链恒定区选自κ型或λ型轻链恒定区。
在一些实施方式中,所述重链恒定区和轻链恒定区的种属来源为牛、马、乳牛、猪、绵羊、山羊、大鼠、小鼠、狗、猫、兔、骆驼、驴、鹿、貂、鸡、鸭、鹅、火鸡、斗鸡或人。
在一些实施方式中,所述重链恒定区和轻链恒定区的种属来源为小鼠。
在一些实施方式中,所述重链恒定区为SEQ ID NO:24或与SEQ ID NO:24具有80%以上同源性的氨基酸序列;所述轻链恒定区为SEQ ID NO:25或与SEQ ID NO:25具有80%以上同源性的氨基酸序列。
需要说明的是,在其他的实施例中,本发明提供的抗体或抗原结合片段的恒定区氨基酸序列可以与上述对应恒定区(SEQ ID NO:24、25)具有至少80%、81%、82%、83%、84%、85%、86%、87%、88%、89%、90%、91%、92%、93%、94%、95%、96%、97%、98%或99%的同源性。
在一些实施方式中,所述抗体的重链的氨基酸序列由SEQ ID NO:17组成;所述抗体的轻链的氨基酸序列由SEQ ID NO:18组成。
在一些实施方式中,所述抗原结合片段选自Fab,Fab',F(ab')2,scFv,Fv,Fd,单链抗体,双价抗体或结构域抗体。
本发明还涉及核酸,所述核酸编码所述抗体或抗原结合片段。
核酸通常是RNA或DNA,核酸分子可以是单链或双链的。当将核酸与另一个核酸序列置于功能关系中时,核酸是“有效连接的”。例如,如果启动子或增强子影响编码序列的转录,那么启动子或增强子有效地连接至所述编码序列。当其连入载体时采用DNA核酸。
本发明还涉及载体,所述载体含有所述核酸。
本发明还涉及细胞,所述细胞含有所述核酸或所述载体。
本发明还涉及一种抗体偶联物,包含所述抗体或抗原结合片段以及与其偶联的偶联部分;
在一些实施方式中,所述偶联部分包括选自纯化标签(如His标签),可检测的标记,例如胶体金、放射性标记、发光物质、有色物质、酶,例如荧光标记、发色团标记、电子致密标记,例如放射性同位素、荧光团、罗丹明及其衍生物、荧光素酶、荧光素、辣根过氧化物酶、碱性磷酸酶、β-半乳糖苷酶、葡糖淀粉酶、溶菌酶、糖类氧化酶、葡萄糖氧化酶、半乳糖氧化酶,和葡萄糖-6-磷酸脱氢酶,生物素/抗生物素蛋白,自旋标记。
在一些实施方式中,所述偶联部分选自磁性微球、塑料微球、塑胶微粒、微孔板、玻璃、毛细管、尼龙和硝酸纤维素膜。
本发明还涉及一种试剂盒或诊断试剂,其包含所述抗体或抗原结合片段或所述抗体偶联物,其中:
可选地,所述试剂盒或诊断试剂还包含结合除登革NS1蛋白以外的抗体或抗原结合片段、抗体偶联物,或融合蛋白。
所述抗体或抗原结合片段或所述抗体偶联物在制备试剂盒或诊断试剂中的用途,同样在本发明的保护范围之内。
下面将结合实施例对本发明的实施方案进行详细描述。
以下实施例中,限制性内切酶、rTaq DNA聚合酶购自Takara公司。MagExtractor-RNA提取试剂盒购自TOYOBO公司。BD SMARTTMRACE cDNAAmplification Kit试剂盒购自Takara公司。pMD-18T载体购自Takara公司。质粒提取试剂盒购自天根公司。引物合成和基因测序由Invitrogen公司完成。
实施例1抗登革NS1蛋白的抗体的制备
1、表达质粒构建
(1)Anti-DF 5M32抗体基因制备
从分泌Anti-DF 5M32单克隆抗体的杂交瘤细胞株中提取mRNA,通过RT-PCR方法获得DNA产物,该产物用rTaq DNA聚合酶进行加A反应后***到pMD-18T载体中,转化到DH5α感受态细胞中,长出菌落后分别取重链(Heavy Chain)及轻链(Light Chain)基因克隆各4个克隆送基因测序公司进行测序。
(2)Anti-DF 5M32抗体可变区基因的序列分析
将上述测序得到的基因序列放在Kabat抗体数据库中进行分析,并利用VNTI11.5软件进行分析确定重链和轻链引物对扩增出的基因都是正确的,其中Light Chain扩增出的基因片段中,VL基因序列为339bp,其前方有57bp的前导肽序列;Heavy Chain引物对扩增出的基因片段中,VH基因序列为351bp,属于VH1基因家族,其前方有57bp的前导肽序列。
(3)重组抗体表达质粒的构建
pcDNATM3.4vector为构建的重组抗体真核表达载体,该表达载体已经引入HindIII、BamHI、EcoRI等多克隆酶切位点,并命名为pcDNA3.4A表达载体,后续简称3.4A表达载体;根据上述pMD-18T中抗体可变区基因测序结果,设计Anti-DF 5M32抗体的VL和VH基因特异性F.引物,两端分别带有HindIII、EcoRI酶切位点和保护碱基,通过PCR扩增方法扩出0.74KB的Light Chain基因片段和1.4kb的Heavy Chain基因片段。
Heavy Chain和Light Chain基因片段分别采用HindIII/EcoRI双酶切,3.4A载体采用HindIII/EcoRI双酶切,将片段和载体纯化回收后Heavy Chain基因和Light Chain基因分别连接3.4A表达载体中,分别得到Heavy Chain和Light Chain的重组表达质粒。
2、稳定细胞株筛选
(1)重组抗体表达质粒瞬时转染CHO细胞,确定表达质粒活性
将步骤1-(3)步骤制备得到的质粒用超纯水稀释至40μg/100μL,调节CHO细胞1.43×107cells/mL于离心管中,100μL上述质粒与700μL细胞混合,转入电转杯,电转,第3、5、7天取样计数,第7天收样检测。
包被液(主要成分NaHCO3)稀释羊抗鼠IgG 1ug/ml进行微孔板包被,每孔100uL,4℃过夜;次日,洗涤液(主要成份Na2HPO4+Nacl)清洗2次,拍干;加入封闭液(20%BSA+80%PBS),每孔120uL,37℃,1h,拍干;加入稀释后的细胞上清,100uL/孔,37℃,60min;甩掉板内液体,拍干,加入20%鼠阴性血封闭,每孔120ul,37℃,1h;甩掉板内液体,拍干,加入稀释的DENV阳性血清,每孔100uL,37℃,40min;洗涤液清洗5次,拍干;加入标记HRP的DENV单克隆抗体,每孔100uL,37℃,30min;加入显色液A液(50uL/孔,主要成份柠檬酸+醋酸钠+乙酰苯胺+过氧化脲),加入显色液B液(50uL/孔,主要成份柠檬酸+EDTA·2Na+TMB+浓HCL),10min;加入终止液(EDTA·2Na+浓H2SO4),50uL/孔;酶标仪上450nm(参考630nm)处读OD值。
结果显示细胞上清稀释1000倍后反应OD仍大于1.0,未加细胞上清孔反应OD小于0.1,表明质粒瞬转后产生的抗体对DENV抗原有活性。
(2)重组抗体表达质粒线性化
准备下述试剂:Buffer 50μL、步骤1-(3)步骤制备得到的质粒100μg/管、PvuⅠ酶10μL、无菌水补至500μL,37℃水浴酶切过夜;先用等体积酚/氯仿/异戊醇(下层)25:24:1,再用氯仿(水相)依次进行抽提;0.1倍体积(水相)3M醋酸钠和2倍体积乙醇冰上沉淀,70%乙醇漂洗沉淀,去除有机溶剂,待乙醇挥发完全用适量的灭菌水进行复融,最后进行浓度的测定。
(3)重组抗体表达质粒稳定转染,加压筛选稳定细胞株
步骤2-(2)步骤制备得到的质粒用超纯水稀释至40μg/100μL,调节CHO细胞1.43×107cells/mL于离心管中,100μL上述质粒与700μL细胞混合,转入电转杯,电转,次日计数;25μmol/L MSX 96孔加压培养约25天。
显微镜下观察标记长有细胞的克隆孔,并记录汇合度;取培养上清,送样检测;挑选抗体浓度、相对浓度高的细胞株转24孔,3天左右转6孔;3天后保种批培,调整细胞密度0.5×106cells/mL,2.2mL进行批培养,细胞密度0.3×106cells/mL,2mL进行保种;7天6孔批培上清送样检测,挑选抗体浓度及细胞直径较小的细胞株转TPP保种传代。
3、重组抗体生产
(1)细胞扩培
细胞复苏之后先在125mL规格的摇瓶中培养,接种体积为30mL,培养基为100%Dynamis培养基,放置于转速120r/min,温度为37℃,二氧化碳为8%的摇床中。培养72h,以50万cells/mL接种密度接种扩培,扩培体积根据生产需求进行计算,培养基为100%Dynamis培养基。之后每72h扩培一次。当细胞量满足生产需求时,严格控制接种密度为50万cells/mL左右进行生产。
(2)摇瓶生产及纯化
摇瓶参数:转速120r/min,温度为37℃,二氧化碳为8%。流加补料:在摇瓶中培养至72h时开始每天补料,HyCloneTM Cell BoostTM Feed 7a每天流加初始培养体积的3%,Feed 7b每天流加量为初始培养体积的千分之一,一直补到第12天(第12天补料)。葡萄糖在第六天补加3g/L。第13天收样。用proteinA亲和层析柱进行亲和纯化。取6.6μg纯化的抗体进行还原性SDS-PAGE,电泳图如图所示。在还原性SDS-PAGE后显示两条带,1条Mr为50KD(重链),另一条Mr为28KD(轻链)。
经上述步骤获得的DF-5M32RMb1的HCDR1-3的氨基酸序列分别如SEQ ID NO.1-3所示;LCDR1-3的氨基酸序列分别如SEQ ID NO.4-6所示。重链可变区、轻链可变区、重链及轻链的氨基酸序列分别如SEQ ID NO.15-18所示。
对DF-5M32RMb1的结构进行分析,并进行突变引物设计,重复步骤1-(3)至3-(2),经活性鉴定,筛选得到DF-8F13RMb2-4。经测序分析,DF-8F13RMb2-4的重链可变区分别如SEQ ID NO.21-23所示,重链恒定区如SEQ ID NO.24所示,轻链与DF-5M32RMb1相同。
实施例2亲和力分析及活性鉴定
1、亲和力分析
利用AMC传感器,纯化出来的抗体用PBST稀释到10ug/ml,DENV-IV抗原(一种NS1蛋白,购自菲鹏)用PBST进行梯度稀释;
运行流程:缓冲液1(PBST)中平衡60s,抗体溶液中固化抗体300s,缓冲液2(PBST)中孵育180s,抗原溶液中结合420s,缓冲液2中解离1200s,用10mM pH 1.69GLY溶液及缓冲液3进行传感器再生,输出数据。
表1
样品名称 | KD(M) | Kon(1/Ms) | Kdis(1/s) |
对照抗体 | 8.11E-07 | 2.34E+03 | 1.90E-03 |
DF-5M32RMb1 | 5.96E-08 | 2.14E+04 | 1.28E-03 |
DF-5M32RMb2 | 5.78E-08 | 3.19E+04 | 1.84E-03 |
DF-5M32RMb3 | 6.36E-08 | 2.93E+04 | 1.86E-03 |
DF-5M32RMb4 | 5.29E-08 | 3.32E+04 | 1.76E-03 |
注:KD表示平衡解离常数即亲和力;Kon表示结合速率常数;Kdis表示解离速率常数。
2、活性鉴定
包被液(主要成分NaHCO3)稀释羊抗鼠IgG 1ug/ml进行微孔板包被,每孔100uL,4℃过夜;次日,洗涤液(主要成份Na2HPO4+Nacl)清洗2次,拍干;加入封闭液(20%BSA+80%PBS),每孔120uL,37℃,1h,拍干;加入稀释后的纯化抗体,100uL/孔,37℃,60min;甩掉板内液体,拍干,加入20%鼠阴性血封闭,每孔120ul,37℃,1h;甩掉板内液体,拍干,加入稀释的DENV阳性血清,每孔100uL,37℃,40min;洗涤液清洗5次,拍干;加入标记HRP的DENV单克隆抗体(与纯化抗体能配对的,购自菲鹏),每孔100uL,37℃,30min;加入显色液A液(50uL/孔),加入显色液B液(50uL/孔),10min;加入终止液,50uL/孔;酶标仪上450nm(参考630nm)处读OD值。
表2
样品浓度(ng/ml) | 12.5 | 6.25 | 3.125 | 1.5625 | 0.78125 | 0 |
对照抗体 | 1.537 | 0.996 | 0.692 | 0.480 | 0.317 | 0.045 |
DF-5M32RMb1 | 2.098 | 1.520 | 0.963 | 0.654 | 0.489 | 0.039 |
DF-5M32RMb2 | 2.042 | 1.474 | 0.960 | 0.603 | 0.471 | 0.031 |
DF-5M32RMb3 | 1.965 | 1.496 | 0.952 | 0.622 | 0.479 | 0.043 |
DF-5M32RMb4 | 2.013 | 1.487 | 0.923 | 0.631 | 0.482 | 0.032 |
实施例3稳定性考核
将实施例1制备得到的单克隆抗体置于4℃(冰箱)、-80℃(冰箱)、37℃(恒温箱)放置21天,取7天、14天、21天样品进行状态观察,并对放置21天的样品进行活性检测(利用酶免检测OD结果考核样品的活性)。
DF-5M32RMb1稳定性测试结果如表3所示,结果显示,DF-5M32RMb1至DF-5M32RMb4在三种考核条件下抗体放置21天均未见明显蛋白状态变化,活性也未随考核温度的升高呈下降趋势,说明本发明制备得到的自产抗体稳定性好。
表3
样品浓度(ng/mL) | 6.25 | 3.125 | 0 |
4℃,21天样品 | 1.421 | 0.897 | 0.041 |
-80℃,21天样品 | 1.469 | 0.811 | 0.033 |
37℃,21天样品 | 1.395 | 0.803 | 0.039 |
上述实施例为本发明较佳的实施方式,但本发明的实施方式并不受上述实施例的限制,其他的任何未背离本发明的精神实质与原理下所作的改变、修饰、替代、组合、简化,均应为等效的置换方式,都包含在本发明的保护范围之内。
SEQUENCE LISTING
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Gly Val Pro Asp Arg Phe Thr Gly Ser Gly Ser Gly Thr Glu Phe Thr
1 5 10 15
Leu Lys Ile Ser Arg Val Glu Ala Glu Asp Leu Gly Val Tyr Tyr Cys
20 25 30
<210> 14
<211> 12
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 14
Phe Gly Thr Gly Thr Asn Leu Glu Leu Lys
1 5 10
<210> 15
<211> 117
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 15
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Ile Asn Tyr
20 25 30
Trp Met Gln Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Ala Ile Tyr Pro Gly Asp Gly Asp Thr Arg Tyr Thr Gln Asn Phe
50 55 60
Lys Gly Lys Ala Ala Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Thr Gly Thr Glu Gly Ile Leu Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Ser Ser
115
<210> 16
<211> 112
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 16
Asp Ala Val Met Thr Gln Thr Pro Leu Thr Leu Ser Val Leu Ile Gly
1 5 10 15
Gln Pro Ala Ser Leu Ser Cys Lys Ser Ser Gln Ser Leu Leu Glu Ser
20 25 30
Asp Gly Lys Thr Tyr Leu Asn Trp Leu Phe Gln Arg Pro Gly Gln Ser
35 40 45
Pro Lys Arg Leu Ile Tyr Leu Val Ser Lys Leu Glu Ser Gly Val Pro
50 55 60
Asp Arg Phe Thr Gly Ser Gly Ser Gly Thr Glu Phe Thr Leu Lys Ile
65 70 75 80
Ser Arg Val Glu Ala Glu Asp Leu Gly Val Tyr Tyr Cys Trp Gln Ala
85 90 95
Thr His His Pro Leu Thr Phe Gly Thr Gly Thr Asn Leu Glu Leu Lys
100 105 110
<210> 17
<211> 441
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 17
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Ile Asn Tyr
20 25 30
Trp Met Gln Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Ala Ile Tyr Pro Gly Asp Gly Asp Thr Arg Tyr Thr Gln Asn Phe
50 55 60
Lys Gly Lys Ala Ala Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Thr Gly Thr Glu Gly Ile Leu Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Ser Ser Ala Lys Thr Thr Pro Pro Ser Val Tyr Pro Leu
115 120 125
Ala Pro Gly Ser Ala Ala Gln Thr Asn Ser Met Val Thr Leu Gly Cys
130 135 140
Leu Val Lys Gly Tyr Phe Pro Glu Pro Val Thr Val Thr Trp Asn Ser
145 150 155 160
Gly Ser Leu Ser Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser
165 170 175
Asp Leu Tyr Thr Leu Ser Ser Ser Val Thr Val Pro Ser Ser Thr Trp
180 185 190
Pro Ser Gln Thr Val Thr Cys Asn Val Ala His Pro Ala Ser Ser Thr
195 200 205
Lys Val Asp Lys Lys Ile Val Pro Arg Asp Cys Gly Cys Lys Pro Cys
210 215 220
Ile Cys Thr Val Pro Glu Val Ser Ser Val Phe Ile Phe Pro Pro Lys
225 230 235 240
Pro Lys Asp Val Leu Thr Ile Thr Leu Thr Pro Lys Val Thr Cys Val
245 250 255
Val Val Asp Ile Ser Lys Asp Asp Pro Glu Val Gln Phe Ser Trp Phe
260 265 270
Val Asp Asp Val Glu Val His Thr Ala Gln Thr Lys Pro Arg Glu Glu
275 280 285
Gln Phe Asn Ser Thr Phe Arg Ser Val Ser Glu Leu Pro Ile Met His
290 295 300
Gln Asp Trp Leu Asn Gly Lys Glu Phe Lys Cys Arg Val Asn Ser Ala
305 310 315 320
Ala Phe Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys Thr Lys Gly Arg
325 330 335
Pro Lys Ala Pro Gln Val Tyr Thr Ile Pro Pro Pro Lys Glu Gln Met
340 345 350
Ala Lys Asp Lys Val Ser Leu Thr Cys Met Ile Thr Asn Phe Phe Pro
355 360 365
Glu Asp Ile Thr Val Glu Trp Gln Trp Asn Gly Gln Pro Ala Glu Asn
370 375 380
Tyr Lys Asn Thr Gln Pro Ile Met Asp Thr Asp Gly Ser Tyr Phe Val
385 390 395 400
Tyr Ser Lys Leu Asn Val Gln Lys Ser Asn Trp Glu Ala Gly Asn Thr
405 410 415
Phe Thr Cys Ser Val Leu His Glu Gly Leu His Asn His His Thr Glu
420 425 430
Lys Ser Leu Ser His Ser Pro Gly Lys
435 440
<210> 18
<211> 218
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 18
Asp Ala Val Met Thr Gln Thr Pro Leu Thr Leu Ser Val Leu Ile Gly
1 5 10 15
Gln Pro Ala Ser Leu Ser Cys Lys Ser Ser Gln Ser Leu Leu Glu Ser
20 25 30
Asp Gly Lys Thr Tyr Leu Asn Trp Leu Phe Gln Arg Pro Gly Gln Ser
35 40 45
Pro Lys Arg Leu Ile Tyr Leu Val Ser Lys Leu Glu Ser Gly Val Pro
50 55 60
Asp Arg Phe Thr Gly Ser Gly Ser Gly Thr Glu Phe Thr Leu Lys Ile
65 70 75 80
Ser Arg Val Glu Ala Glu Asp Leu Gly Val Tyr Tyr Cys Trp Gln Ala
85 90 95
Thr His His Pro Leu Thr Phe Gly Thr Gly Thr Asn Leu Glu Leu Lys
100 105 110
Arg Ala Asp Ala Ala Pro Thr Val Ser Ile Phe Pro Pro Ser Ser Glu
115 120 125
Gln Leu Thr Ser Gly Gly Ala Ser Val Val Cys Phe Leu Asn Asn Phe
130 135 140
Tyr Pro Lys Asp Ile Asn Val Lys Trp Lys Ile Asp Gly Ser Glu Arg
145 150 155 160
Gln Asn Gly Val Leu Asn Ser Trp Thr Asp Gln Asp Ser Lys Asp Ser
165 170 175
Thr Tyr Ser Met Ser Ser Thr Leu Thr Leu Thr Lys Asp Glu Tyr Glu
180 185 190
Arg His Asn Ser Tyr Thr Cys Glu Ala Thr His Lys Thr Ser Thr Ser
195 200 205
Pro Ile Val Lys Ser Phe Asn Arg Asn Glu
210 215
<210> 19
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 19
Gly Thr Glu Gly Leu Leu Asp Tyr
1 5
<210> 20
<211> 30
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 20
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Leu
20 25 30
<210> 21
<211> 117
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 21
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Leu Asn Tyr
20 25 30
Trp Met Gln Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Ala Ile Tyr Pro Gly Asp Gly Asp Thr Arg Tyr Thr Gln Asn Phe
50 55 60
Lys Gly Lys Ala Ala Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Thr Gly Thr Glu Gly Leu Leu Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Ser Ser
115
<210> 22
<211> 117
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 22
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Leu Asn Tyr
20 25 30
Trp Met Gln Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Ala Ile Tyr Pro Gly Asp Gly Asp Thr Arg Tyr Thr Gln Asn Phe
50 55 60
Lys Gly Lys Ala Ala Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Thr Gly Thr Glu Gly Ile Leu Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Ser Ser
115
<210> 23
<211> 117
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 23
Gln Val Gln Leu Gln Gln Ser Gly Ala Glu Leu Ala Arg Pro Gly Ala
1 5 10 15
Ser Val Lys Leu Ser Cys Lys Ala Ser Gly Tyr Thr Phe Ile Asn Tyr
20 25 30
Trp Met Gln Trp Val Lys Gln Arg Pro Gly Gln Gly Leu Glu Trp Ile
35 40 45
Gly Ala Ile Tyr Pro Gly Asp Gly Asp Thr Arg Tyr Thr Gln Asn Phe
50 55 60
Lys Gly Lys Ala Ala Leu Thr Ala Asp Lys Ser Ser Ser Thr Ala Tyr
65 70 75 80
Met Gln Leu Ser Ser Leu Ala Ser Glu Asp Ser Ala Val Tyr Tyr Cys
85 90 95
Ala Thr Gly Thr Glu Gly Leu Leu Asp Tyr Trp Gly Gln Gly Thr Ser
100 105 110
Val Thr Val Ser Ser
115
<210> 24
<211> 324
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 24
Ala Lys Thr Thr Pro Pro Ser Val Tyr Pro Leu Ala Pro Gly Ser Ala
1 5 10 15
Ala Gln Thr Asn Ser Met Val Thr Leu Gly Cys Leu Val Lys Gly Tyr
20 25 30
Phe Pro Glu Pro Val Thr Val Thr Trp Asn Ser Gly Ser Leu Ser Ser
35 40 45
Gly Val His Thr Phe Pro Ala Val Leu Gln Ser Asp Leu Tyr Thr Leu
50 55 60
Ser Ser Ser Val Thr Val Pro Ser Ser Thr Trp Pro Ser Gln Thr Val
65 70 75 80
Thr Cys Asn Val Ala His Pro Ala Ser Ser Thr Lys Val Asp Lys Lys
85 90 95
Ile Val Pro Arg Asp Cys Gly Cys Lys Pro Cys Ile Cys Thr Val Pro
100 105 110
Glu Val Ser Ser Val Phe Ile Phe Pro Pro Lys Pro Lys Asp Val Leu
115 120 125
Thr Ile Thr Leu Thr Pro Lys Val Thr Cys Val Val Val Asp Ile Ser
130 135 140
Lys Asp Asp Pro Glu Val Gln Phe Ser Trp Phe Val Asp Asp Val Glu
145 150 155 160
Val His Thr Ala Gln Thr Lys Pro Arg Glu Glu Gln Phe Asn Ser Thr
165 170 175
Phe Arg Ser Val Ser Glu Leu Pro Ile Met His Gln Asp Trp Leu Asn
180 185 190
Gly Lys Glu Phe Lys Cys Arg Val Asn Ser Ala Ala Phe Pro Ala Pro
195 200 205
Ile Glu Lys Thr Ile Ser Lys Thr Lys Gly Arg Pro Lys Ala Pro Gln
210 215 220
Val Tyr Thr Ile Pro Pro Pro Lys Glu Gln Met Ala Lys Asp Lys Val
225 230 235 240
Ser Leu Thr Cys Met Ile Thr Asn Phe Phe Pro Glu Asp Ile Thr Val
245 250 255
Glu Trp Gln Trp Asn Gly Gln Pro Ala Glu Asn Tyr Lys Asn Thr Gln
260 265 270
Pro Ile Met Asp Thr Asp Gly Ser Tyr Phe Val Tyr Ser Lys Leu Asn
275 280 285
Val Gln Lys Ser Asn Trp Glu Ala Gly Asn Thr Phe Thr Cys Ser Val
290 295 300
Leu His Glu Gly Leu His Asn His His Thr Glu Lys Ser Leu Ser His
305 310 315 320
Ser Pro Gly Lys
<210> 25
<211> 106
<212> PRT
<213> Artificial Sequence
<220>
<223> 人工序列
<400> 25
Arg Ala Asp Ala Ala Pro Thr Val Ser Ile Phe Pro Pro Ser Ser Glu
1 5 10 15
Gln Leu Thr Ser Gly Gly Ala Ser Val Val Cys Phe Leu Asn Asn Phe
20 25 30
Tyr Pro Lys Asp Ile Asn Val Lys Trp Lys Ile Asp Gly Ser Glu Arg
35 40 45
Gln Asn Gly Val Leu Asn Ser Trp Thr Asp Gln Asp Ser Lys Asp Ser
50 55 60
Thr Tyr Ser Met Ser Ser Thr Leu Thr Leu Thr Lys Asp Glu Tyr Glu
65 70 75 80
Arg His Asn Ser Tyr Thr Cys Glu Ala Thr His Lys Thr Ser Thr Ser
85 90 95
Pro Ile Val Lys Ser Phe Asn Arg Asn Glu
100 105
Claims (25)
1.一种抗登革病毒或其NS1蛋白的抗体或其抗原结合片段,其特征在于,所述抗体或其抗原结合片段包含以下CDRs:
HCDR1,其氨基酸序列如SEQ ID NO.1所示;
HCDR2,其氨基酸序列如SEQ ID NO.2所示;
HCDR3,其氨基酸序列如SEQ ID NO.3或SEQ ID NO.19所示;
LCDR1,其氨基酸序列如SEQ ID NO.4所示;
LCDR2,其氨基酸序列如SEQ ID NO.5所示;
LCDR3,其氨基酸序列如SEQ ID NO.6所示。
2.根据权利要求1所述的抗体或其抗原结合片段,所述的抗体或其抗原结合片段还包含重链可变区的框架区HFR1、HFR2、HFR3和HFR4,和轻链可变区的框架区LFR1、LFR2、LFR3和LFR4,所述
HFR1包含选自SEQ ID NO:7、SEQ ID NO:20、与SEQ ID NO:7具有90%以上同源性或与SEQ ID NO:20具有80%以上同源性的任一氨基酸序列;
HFR2包含SEQ ID NO:8或与SEQ ID NO:8具有80%以上同源性的氨基酸序列;
HFR3包含SEQ ID NO:9或与SEQ ID NO:9具有80%以上同源性的氨基酸序列;
HFR4包含SEQ ID NO:10或与SEQ ID NO:10具有80%以上同源性的氨基酸序列;和
LFR1包含SEQ ID NO:11或与SEQ ID NO:11具有80%以上同源性的氨基酸序列;
LFR2包含SEQ ID NO:12或与SEQ ID NO:12具有80%以上同源性的氨基酸序列;
LFR3包含SEQ ID NO:13或与SEQ ID NO:13具有80%以上同源性的氨基酸序列;
LFR4包含SEQ ID NO:14或与SEQ ID NO:14具有80%以上同源性的氨基酸序列。
3.一种抗登革病毒或其NS1蛋白的抗体或其抗原结合片段,其特征在于,所述抗体或其抗原结合片段包含重链可变区和轻链可变区,所述重链可变区包含权利要求1所述的HCDR1-3和权利要求2所述的HFR1-4,所述轻链可变区包含权利要求1所述的LCDR1-3和权利要求2所述的LFR1-4。
4.一种抗登革病毒或其NS1蛋白的抗体或其抗原结合片段,其特征在于,其重链可变区包含选自SEQ ID NO:15、SEQ ID NO:21-23任一所示的氨基酸序列,或由其组成;
其轻链可变区包含SEQ ID NO:16所示的氨基酸序列,或由其组成。
5.根据权利要求1至4任一所述的抗体或其抗原结合片段,还包含恒定区。
6.根据权利要求5所述的抗体或其抗原结合片段,其特征在于,所述恒定区包括重链恒定区和/或轻链恒定区。
7.根据权利要求6所述的抗体或其抗原结合片段,其特征在于,所述重链恒定区选自IgG1、IgG2、IgG3、IgG4、IgA、IgM、IgE或IgD的重链恒定区;所述轻链恒定区选自κ型或λ型轻链恒定区。
8.根据权利要求5所述的抗体或其抗原结合片段,其特征在于,所述恒定区的种属来源为牛、马、猪、绵羊、山羊、大鼠、小鼠、狗、猫、兔、骆驼、驴、鹿、貂、鸡、鸭、鹅或人。
9.根据权利要求8所述的抗体或其抗原结合片段,其特征在于,所述牛为乳牛。
10.根据权利要求8所述的抗体或其抗原结合片段,其特征在于,所述鸡为火鸡或斗鸡。
11.根据权利要求8所述的抗体或其抗原结合片段,其特征在于,所述恒定区的种属来源为小鼠。
12. 根据权利要求6所述的抗体或其抗原结合片段,其特征在于,所述重链恒定区为SEQ ID NO:24或与SEQ ID NO:24具有80%以上同源性的氨基酸序列;所述轻链恒定区为SEQ ID NO:25或与SEQ ID NO:25具有80%以上同源性的氨基酸序列。
13.一种核酸,其特征在于,所述核酸编码权利要求1至12任一所述的抗体或其抗原结合片段。
14.一种细胞,其特征在于,所述细胞包含权利要求13所述的核酸。
15.一种制备权利要求1至12任一所述的抗体或其抗原结合片段的方法,其特征在于,所述方法包括培养权利要求14所述的细胞。
16.一种抗体偶联物,其特征在于,所述抗体偶联物包含权利要求1至12任一所述的抗体或其抗原结合片段以及与其偶联的偶联部分。
17.根据权利要求16所述的抗体偶联物,其特征在于,所述偶联部分选自纯化标签或可检测的标记。
18.根据权利要求17所述的抗体偶联物,其特征在于,所述偶联部分选自胶体金、放射性标记、发光物质、有色物质和酶中的一种或多种。
19.根据权利要求17所述的抗体偶联物,其特征在于,所述偶联部分选自荧光标记、发色团标记和电子致密标记中的一种或多种。
20.根据权利要求17所述的抗体偶联物,其特征在于,所述偶联部分选自放射性同位素、荧光团、罗丹明及其衍生物、荧光素酶、荧光素、辣根过氧化物酶、碱性磷酸酶、β-半乳糖苷酶、葡糖淀粉酶、溶菌酶、糖类氧化酶、生物素、抗生物素蛋白和自旋标记的一种或多种。
21.根据权利要求20所述的抗体偶联物,其特征在于,所述偶联部分选自葡萄糖氧化酶、半乳糖氧化酶,和葡萄糖-6-磷酸脱氢酶中的一种或多种。
22.根据权利要求16所述的抗体偶联物,其特征在于,所述偶联部分选自磁性微球、塑料微球、塑胶微粒、微孔板、玻璃、毛细管、尼龙和硝酸纤维素膜。
23.一种试剂盒或诊断试剂,其特征在于,所述试剂盒或诊断试剂包含权利要求1至12任一所述的抗体或其抗原结合片段或权利要求16~22任一项所述的抗体偶联物。
24.根据权利要求23所述的试剂盒或诊断试剂,其特征在于,所述试剂盒或诊断试剂还包含结合除登革NS1蛋白以外的抗原片段的抗体或其抗原结合片段、抗体偶联物,或融合蛋白。
25.权利要求1至12任一所述的抗体或其抗原结合片段或权利要求16~22任一项所述的抗体偶联物在制备试剂盒或诊断试剂中的用途。
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CN109053882A (zh) * | 2018-08-28 | 2018-12-21 | 东莞市朋志生物科技有限公司 | 一种ns1蛋白的结合蛋白以及应用 |
CN109081869A (zh) * | 2018-08-28 | 2018-12-25 | 东莞市朋志生物科技有限公司 | Ns1蛋白的结合蛋白 |
CN112194712A (zh) * | 2019-11-07 | 2021-01-08 | 中国科学院微生物研究所 | 一种寨卡/登革疫苗及其应用 |
CN111718416A (zh) * | 2020-06-25 | 2020-09-29 | 菲鹏生物股份有限公司 | 抗硫氧还蛋白的抗体、其应用和诊断试剂盒 |
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